{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363388844133747712.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1046/j.1365-2958.1998.00921.x"}},{"identifier":{"@type":"URI","@value":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1365-2958.1998.00921.x"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-2958.1998.00921.x"}},{"identifier":{"@type":"URI","@value":"https://onlinelibrary.wiley.com/doi/full-xml/10.1046/j.1365-2958.1998.00921.x"}},{"identifier":{"@type":"NAID","@value":"80010427723"}}],"dc:title":[{"@value":"<i>Bacillus subtilis</i> contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:p>Fur (ferric uptake regulator) proteins control iron uptake in many Gram‐negative bacteria. Although Fur homologues have been identified in Gram‐positive bacteria, their roles in gene regulation are unknown. Genome sequencing has revealed three <jats:italic>fur</jats:italic> homologues in <jats:italic>Bacillus subtilis</jats:italic>: <jats:italic>yqkL</jats:italic>, <jats:italic>yqfV</jats:italic> and <jats:italic>ygaG</jats:italic>. We demonstrate that <jats:italic>yqkL</jats:italic> encodes an iron uptake repressor: both siderophore biosynthesis and transcription of ferri‐siderophore uptake genes is constitutive in the <jats:italic>yqkL</jats:italic> mutant. Thus, <jats:italic>yqkL</jats:italic> encodes a repressor that is functionally as well as structurally related to Fur. <jats:italic>B. subtilis</jats:italic> peroxide stress genes are induced by either H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> or by metal ion limitation. Previous genetic studies defined a regulatory locus, <jats:italic>perR</jats:italic>, postulated to encode the peroxide regulon repressor. We demonstrate that a <jats:italic>ygaG</jats:italic> mutant has the <jats:italic>perR</jats:italic> phenotype: it is highly resistant to peroxides and overexpresses catalase, alkyl hydroperoxide reductase and the DNA binding protein MrgA. Nine spontaneous <jats:italic>perR</jats:italic> mutations, isolated by virtue of their ability to derepress <jats:italic>mrgA</jats:italic> transcription in the presence of manganous ion, all contain sequence changes in the <jats:italic>ygaG</jats:italic> locus and can be complemented by the cloned <jats:italic>ygaG</jats:italic> gene. Thus, <jats:italic>ygaG</jats:italic> encodes the peroxide regulon repressor and is allelic with <jats:italic>perR</jats:italic>.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1383388844133747713","@type":"Researcher","foaf:name":[{"@value":"Nada Bsat"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388844133747714","@type":"Researcher","foaf:name":[{"@value":"Andrew Herbig"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388844133747715","@type":"Researcher","foaf:name":[{"@value":"Lilliam Casillas‐Martinez"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388844133747712","@type":"Researcher","foaf:name":[{"@value":"Peter Setlow"}]},{"@id":"https://cir.nii.ac.jp/crid/1383388844133747840","@type":"Researcher","foaf:name":[{"@value":"John D. Helmann"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"0950382X"},{"@type":"EISSN","@value":"13652958"}],"prism:publicationName":[{"@value":"Molecular Microbiology"}],"dc:publisher":[{"@value":"Wiley"}],"prism:publicationDate":"1998-07","prism:volume":"29","prism:number":"1","prism:startingPage":"189","prism:endingPage":"198"},"reviewed":"false","dc:rights":["http://onlinelibrary.wiley.com/termsAndConditions#vor"],"url":[{"@id":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1365-2958.1998.00921.x"},{"@id":"https://onlinelibrary.wiley.com/doi/pdf/10.1046/j.1365-2958.1998.00921.x"},{"@id":"https://onlinelibrary.wiley.com/doi/full-xml/10.1046/j.1365-2958.1998.00921.x"}],"createdAt":"2003-03-12","modifiedAt":"2023-09-11","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050001335835677184","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Protein oxidation mediated by heme-induced active site conversion specific for heme-regulated transcription factor, iron response regulator"}]},{"@id":"https://cir.nii.ac.jp/crid/1360846641534313600","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Redox-Dependent Dynamics in Heme-Bound Bacterial Iron Response Regulator (Irr) Protein"}]},{"@id":"https://cir.nii.ac.jp/crid/1360848660898825856","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Silica-Induced Protein (Sip) in Thermophilic Bacterium Thermus thermophilus Responds to Low Iron Availability"}]},{"@id":"https://cir.nii.ac.jp/crid/1390001204425343360","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"細菌の酸化ストレス防御システムと酸化系抗菌剤の作用メカニズム"},{"@language":"en","@value":"Bacterial Defense Systems against Oxidative Stress and the Mode of Action of Oxidative Antimicrobial Agents"},{"@language":"ja-Kana","@value":"サイキン ノ サンカ ストレス ボウギョ システム ト サンカケイ コウキンザイ ノ サヨウ メカニズム"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282679604333824","@type":"Article","relationType":["isReferencedBy","isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Proteases of a Bacillus subtilis Clinical Isolate Facilitate Swarming and Siderophore-Mediated Iron Uptake via Proteolytic Cleavage of Transferrin"}]},{"@id":"https://cir.nii.ac.jp/crid/1390282681452697216","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Cloning, Nucleotide Sequence, and Disruption of Streptococcus mutans Glutathione Reductase Gene (gor)."},{"@value":"Cloning, Nucleotide Sequence, and Disruption of<i>Streptococcus mutans</i>Glutathione Reductase Gene (<i>gor</i>)"}]},{"@id":"https://cir.nii.ac.jp/crid/1520010380368823168","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"Overexpression of FurA in Anabaena sp. PCC 7120 reveals new targets for this regulator involved in photosynthesis, iron uptake and cellular morphology"},{"@language":"ja-Kana","@value":"Overexpression of FurA in Anabaena sp PCC 7120 reveals new targets for this regulator involved in photosynthesis iron uptake and cellular morphology"}]},{"@id":"https://cir.nii.ac.jp/crid/1522825129598912000","@type":"Article","relationType":["isCitedBy"],"jpcoar:relatedTitle":[{"@value":"Response to Oxidative Stress Involves a Novel Peroxiredoxin Gene in the Unicellular Cyanobacterium Synechocystis sp. PCC 6803"},{"@language":"ja-Kana","@value":"Response to Oxidative Stress Involves a Novel Peroxiredoxin Gene in the Unicellular Cyanobacterium Synechocystis sp PCC 6803"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1046/j.1365-2958.1998.00921.x"},{"@type":"CIA","@value":"80010427723"},{"@type":"CROSSREF","@value":"10.1038/srep18703_references_DOI_QbhzAWEBXY5XVgYldX61bKi6aB0"},{"@type":"CROSSREF","@value":"10.1021/acs.biochem.6b00512_references_DOI_QbhzAWEBXY5XVgYldX61bKi6aB0"},{"@type":"CROSSREF","@value":"10.1248/bpb.29.850_references_DOI_QbhzAWEBXY5XVgYldX61bKi6aB0"},{"@type":"CROSSREF","@value":"10.1128/aem.04027-15_references_DOI_QbhzAWEBXY5XVgYldX61bKi6aB0"}]}